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dc.contributor.advisorRussell, David H.en_US
dc.creatorLucas, Jessica Elaineen_US
dc.date.accessioned2004-09-30T01:41:23Z
dc.date.available2004-09-30T01:41:23Z
dc.date.created2003-12en_US
dc.date.issued2004-09-30
dc.identifier.urihttp://hdl.handle.net/1969.1/66
dc.description.abstractPeptide mass fingerprinting (PMF) of protein digests is a widely-accepted method for protein identification in MS-based proteomic studies. Matrix-assisted laser desorption/ionization mass spectrometry (MALDI) is the technique of choice in PMF experiments. The success of protein identification in a PMF experiment is directly related to the amount of amino acid sequence coverage. In an effort to increase the amount of sequence information obtained in a MALDI PMF experiment, performic acid oxidation is performed on tryptic digests of known proteins. Performic acid was chosen as the chemical oxidant due to the ease of use and to the selective oxidation of cysteine, methionine, and tryptophan residues. In experiments performed in our laboratory, performic acid oxidation either increased or did not affect protein sequence coverage in PMF experiments when oxidized tryptic digests were analyzed by MALDI. Negative mode MALDI data were acquired, as well as positive mode MALDI data, due to the enhanced ionization of cysteic acid-containing peptides in negative mode. Furthermore, the confidence in a protein match is increased by observation of mass shifts indicative of cysteine, methionine, and/or tryptophan in oxidized peptide ion signals when comparing MALDI spectra prior to performic acid oxidation and after oxidation due to the low abundance of these residues in the majority of all known and hypothetical proteins.en_US
dc.format.extent1657002 bytes
dc.format.extent86509 bytes
dc.format.mediumelectronicen_US
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_USen_US
dc.publisherTexas A&M Universityen_US
dc.subjectpeptide mass fingerprinten_US
dc.subjecttryptic peptidesen_US
dc.subjectchemical oxidationen_US
dc.subjectMALDI-MSen_US
dc.subjectpercent sequence coverageen_US
dc.titleChemical oxidation of tryptic digests to improve sequence coverage in peptide mass fingerprint protein identificationen_US
dc.typeBooken
dc.typeThesisen
thesis.degree.departmentChemistryen_US
thesis.degree.disciplineChemistryen_US
thesis.degree.grantorTexas A&M Universityen_US
thesis.degree.nameMaster of Scienceen_US
thesis.degree.levelMastersen_US
dc.contributor.committeeMemberSchweikert, Emile A.en_US
dc.contributor.committeeMemberSummers, Max D.en_US
dc.contributor.committeeMemberVigh, Gyulaen_US
dc.type.genreElectronic Thesisen_US
dc.type.materialtexten_US
dc.format.digitalOriginborn digitalen_US


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